Coarse-grain simulations on NMR conformational ensembles highlight functional residues in proteins.

ABSTRACT: Dynamics are a key feature of protein function, and this is especially true of gating residues, which occupy cavity or tunnel lining positions in the protein structure, and will reversibly switch between open and closed conformations in order to control the diffusion of small molecules within a protein's internal matrix. Earlier work on globins and hydrogenases have shown that these gating residues can be detected using a multiscale scheme combining all-atom classic molecular dynamics simulations and coarse-grain calculations of the resulting conformational ensemble mechanical properties. Here, we show that the structural variations observed in the conformational ensembles produced by NMR spectroscopy experiments are sufficient to induce noticeable mechanical changes in a protein, which in

SUBMITTER: Sacquin-Mora S 

PROVIDER: S-EPMC6685036 | biostudies-literature | 2019 Jul

REPOSITORIES: biostudies-literature